Immunological characterization of the 7-S domain of type IV collagens.
Antisera were raised against the long and short form of mouse and human 7-S collagen and against type IV collagens solubilized by acid extraction or limited digestion with pepsin. All the antisera showed strong binding for 7-S collagen in radioimmunoassays demonstrating that the 7-S domain which serves as a cross-linking region of type IV collagen is the most immunogenic portion of the molecule. Cross-reaction studies and analysis of fragments showed a complex antigenic structure including some determinants common to the long and short form of 7-S collagen and others unique for the long form. Purified antibodies against 7-S collagen reacted in indirect immunofluorescence with almost all basement membranes of the body indicating that the 7-S domain is a common structural element of type IV collagens.
D000818:Animals; D000906:Antibodies / Q000032:analysis; D003094:Collagen / Q000276:immunology*; D003429:Cross Reactions; D005455:Fluorescent Antibody Technique; D006168:Guinea Pigs; D005779:Immunodiffusion; D051379:Mice; D010434:Pepsin A / Q000378:metabolism; D010446:Peptide Fragments / Q000276:immunology; D011817:Rabbits; D011863:Radioimmunoassay
D000906:Antibodies; D010446:Peptide Fragments; D003094:Collagen; D010434:Pepsin A